Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. Interacts (via the C-terminal) with MMP2 (via the C- terminal PEX domain); the interaction inhibits the MMP2 activity. Down-regulated by TGFB1. Belongs to the protease inhibitor I35 (TIMP) family. Note: This description may include information from UniProtKB.
Protein type: Extracellular matrix; Inhibitor protein; Secreted, signal peptide; Cell development/differentiation; Motility/polarity/chemotaxis; Secreted
Molecular Function: integrin binding; metalloendopeptidase inhibitor activity; protein binding; protease binding; metal ion binding; enzyme activator activity
Biological Process: response to drug; regulation of Rap protein signal transduction; negative regulation of metalloenzyme activity; extracellular matrix organization and biogenesis; central nervous system development; response to hormone stimulus; negative regulation of membrane protein ectodomain proteolysis; extracellular matrix disassembly; negative regulation of cell proliferation; positive regulation of MAPKKK cascade; response to cytokine stimulus; negative regulation of Ras protein signal transduction; negative regulation of mitotic cell cycle; positive regulation of adenylate cyclase activity; positive regulation of neuron differentiation; aging
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.